Identification of the Active Site Histidine in the Corrinoid Protein MtrA of the Energy‐Conserving Methyltransferase Complex From <i>Methanobacterium Thermoautotrophicum</i>

Harms, Ulrike; Thauer, Rudolf K.

doi:10.1111/j.1432-1033.1997.00783.x

Cited by 25 publications

(26 citation statements)

References 27 publications

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“…The genomes of Methanosarcina species harbor the mtxXAH genes, which have been proposed to code for a corrinoid-containing enzyme complex that catalyzes the formation of methyl-H 4 MPT from methanol and H 4 MPT and to be involved in methanol oxidation to CO 2 (32). However, mtxXAH homologues are not found in the genome of M. stadtmanae.…”

Section: Resultsmentioning

confidence: 97%

The Genome Sequence of Methanosphaera stadtmanae Reveals Why This Human Intestinal Archaeon Is Restricted to Methanol and H ₂ for Methane Formation and ATP Synthesis

Seedorf²,

et al. 2006

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Methanosphaera stadtmanae has the most restricted energy metabolism of all methanogenic archaea. This human intestinal inhabitant can generate methane only by reduction of methanol with H 2 and is dependent on acetate as a carbon source. We report here the genome sequence of M. stadtmanae, which was found to be composed of 1,767,403 bp with an average G؉C content of 28% and to harbor only 1,534 protein-encoding sequences (CDS). The genome lacks 37 CDS present in the genomes of all other methanogens. Among these are the CDS for synthesis of molybdopterin and for synthesis of the carbon monoxide dehydrogenase/acetylcoenzyme A synthase complex, which explains why M. stadtmanae cannot reduce CO 2 to methane or oxidize methanol to CO 2 and why this archaeon is dependent on acetate for biosynthesis of cell components. Four sets of mtaABC genes coding for methanol:coenzyme M methyltransferases were found in the genome of M. stadtmanae. These genes exhibit homology to mta genes previously identified in Methanosarcina species. The M. stadtmanae genome also contains at least 323 CDS not present in the genomes of all other archaea. Seventythree of these CDS exhibit high levels of homology to CDS in genomes of bacteria and eukaryotes. These 73 CDS include 12 CDS which are unusually long (>2,400 bp) with conspicuous repetitive sequence elements, 13 CDS which exhibit sequence similarity on the protein level to CDS encoding enzymes involved in the biosynthesis of cell surface antigens in bacteria, and 5 CDS which exhibit sequence similarity to the subunits of bacterial type I and III restriction-modification systems.There are two types of methanogenic archaea, those belonging to the order Methanosarcinales, which contain cytochromes and which can use methanol, methyl amines, acetate, and/or CO 2 plus H 2 as methanogenic substrates, and those belonging to the orders Methanobacteriales, Methanomicrobiales, Methanococcales, and Methanopyrales, which are devoid of cytochromes and which can use CO 2 plus H 2 and/or formate only to fuel anaerobic growth (95, 102). The energy metabolism of both types of methanogens has been investigated in detail (17). However, there are still a few pertinent questions. For example, why is the growth yield on H 2 and CO 2 of methanogens lacking cytochromes considerably lower (Ͻ50%) than that of cytochrome-containing methanogens? The growth yield on H 2 and CO 2 of Methanobrevibacter arboriphilus is 1.3 g/mol methane, whereas that of Methanosarcina barkeri is 7.3 g/mol (101). Could the reason for this be that in cytochrome-containing methanogens two steps in the reduction of CO 2 to methane, methyl transfer from methyl-tetrahydromethanopterin (methyl-H 4 MPT) to coenzyme M and reduction of the heterodisulfide coenzyme M-S-S-coenzyme B (CoM-S-S-CoB) with H 2 , are coupled with energy conservation, whereas in methanogens without cytochromes only one step, the methyltransfer reaction, is coupled? Indeed, methanogens with cytochromes contain a heterodisulfide reductase (HdrDE) that is anchored via a cytoc...

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Section: Resultsmentioning

confidence: 97%

The Genome Sequence of Methanosphaera stadtmanae Reveals Why This Human Intestinal Archaeon Is Restricted to Methanol and H ₂ for Methane Formation and ATP Synthesis

Seedorf²,

et al. 2006

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“…It thus appears that CmuA, whose calculated molecular mass is 67 kDa, represents an unprecedented fusion of two proteins that are expressed as separate but closely associated polypeptides in methyl transfer systems of methanogenic archaea. CmuB, the second methyltransferase-like protein suggested from sequence analysis, showed most sequence identity (30%, Table -methyltetrahydromethanopterin:coenzyme M methyltransferase complex from Methanobacterium thermoautotrophicum, which catalyzes transfer of the methyl group of N 5 -methyltetrahydromethanopterin to the corrinoid protein MtrA (27). CmuB, unlike CmuA, also showed low but significant pairwise identity (23%) to the CH 3 -H 4 folate-binding domain of MetH from E. coli (residues 337-648 in the protein sequence).…”

Section: Resultsmentioning

confidence: 99%

A corrinoid-dependent catabolic pathway for growth of aMethylobacteriumstrain with chloromethane

Vannelli

Meßmer

Studer

et al. 1999

Proc. Natl. Acad. Sci. U.S.A.

103

165

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Methylobacterium sp. strain CM4, an aerobic methylotrophic ␣-proteobacterium, is able to grow with chloromethane as a carbon and energy source. Mutants of this strain that still grew with methanol, methylamine, or formate, but were unable to grow with chloromethane, were previously obtained by miniTn5 mutagenesis. The transposon insertion sites in six of these mutants mapped to two distinct DNA fragments. The sequences of these fragments, which extended over more than 17 kb, were determined. Sequence analysis, mutant properties, and measurements of enzyme activity in cell-free extracts allowed the definition of a multistep pathway for the conversion of chloromethane to formate. The methyl group of chloromethane is first transferred by the protein CmuA (cmu: chloromethane utilization) to a corrinoid protein, from where it is transferred to H 4 folate by CmuB. Both CmuA and CmuB display sequence similarity to methyltransferases of methanogenic archaea. In its C-terminal part, CmuA is also very similar to corrinoid-binding proteins, indicating that it is a bifunctional protein consisting of two domains that are expressed as separate polypeptides in methyl transfer systems of methanogens. The methyl group derived from chloromethane is then processed by means of pterinelinked intermediates to formate by a pathway that appears to be distinct from those already described in Methylobacterium. Remarkable features of this pathway for the catabolism of chloromethane thus include the involvement of a corrinoiddependent methyltransferase system for dehalogenation in an aerobe and a set of enzymes specifically involved in funneling the C1 moiety derived from chloromethane into central metabolism.

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“…The presence of a CO dehydrogenase (cooS) in the BA1 genome also suggests that CO may be used as a carbon source, using a mechanism similar to Methanosarcina and Methanobacterium species (69)(70)(71). Methanol or other methylated compounds may be assimilated via methyl-H 4 MPT by methyl-H 4 MPT methyltransferase (mtrH) and an associated corrinoid protein, similar to the mechanism hypothesized by Harms and Thauer (18). It is also plausible that mtrH and the associated corrinoid protein may donate unknown methyl-groups to coenzyme M as a substrate for methanogenesis.…”

Section: Supplementary Textmentioning

confidence: 96%

Methane metabolism in the archaeal phylum Bathyarchaeota revealed by genome-centric metagenomics

Evans

Parks

Chadwick

et al. 2015

Science

697

580

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Methane cycling gets more diverse The production and consumption of methane by microorganisms play a major role in the global carbon cycle. Although these processes can occur in a range of environments, from animal guts to the deep ocean, these metabolisms are confined to the Archaea. Evans et al. used metagenomics to assemble two nearly complete archaeal genomes from deep groundwater methanogens (see the Perspective by Lloyd). The two reconstructed genomes are members of the recently described Bathyarchaeota and not the phylum to which all previously known methane-metabolizing archaea belonged. Science , this issue p. 434 , see also p. 384

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Identification of the Active Site Histidine in the Corrinoid Protein MtrA of the Energy‐Conserving Methyltransferase Complex From Methanobacterium Thermoautotrophicum

Abstract: The energy-conserving corrinoid-containing MtrA-H complex from Methanobacterium thermoautotrophicum is composed of eight different subunits of which MtrA harbors the corrinoid prosthetic group.

Cited by 25 publications

References 27 publications

The Genome Sequence of Methanosphaera stadtmanae Reveals Why This Human Intestinal Archaeon Is Restricted to Methanol and H ₂ for Methane Formation and ATP Synthesis

The Genome Sequence of Methanosphaera stadtmanae Reveals Why This Human Intestinal Archaeon Is Restricted to Methanol and H ₂ for Methane Formation and ATP Synthesis

A corrinoid-dependent catabolic pathway for growth of aMethylobacteriumstrain with chloromethane

Methane metabolism in the archaeal phylum Bathyarchaeota revealed by genome-centric metagenomics

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Identification of the Active Site Histidine in the Corrinoid Protein MtrA of the Energy‐Conserving Methyltransferase Complex From Methanobacterium Thermoautotrophicum

Abstract: The energy-conserving corrinoid-containing MtrA-H complex from Methanobacterium thermoautotrophicum is composed of eight different subunits of which MtrA harbors the corrinoid prosthetic group.

Cited by 25 publications

References 27 publications

The Genome Sequence of Methanosphaera stadtmanae Reveals Why This Human Intestinal Archaeon Is Restricted to Methanol and H 2 for Methane Formation and ATP Synthesis

The Genome Sequence of Methanosphaera stadtmanae Reveals Why This Human Intestinal Archaeon Is Restricted to Methanol and H 2 for Methane Formation and ATP Synthesis

A corrinoid-dependent catabolic pathway for growth of aMethylobacteriumstrain with chloromethane

Methane metabolism in the archaeal phylum Bathyarchaeota revealed by genome-centric metagenomics

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Resources

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The Genome Sequence of Methanosphaera stadtmanae Reveals Why This Human Intestinal Archaeon Is Restricted to Methanol and H ₂ for Methane Formation and ATP Synthesis

The Genome Sequence of Methanosphaera stadtmanae Reveals Why This Human Intestinal Archaeon Is Restricted to Methanol and H ₂ for Methane Formation and ATP Synthesis